메뉴 건너뛰기




Volumn 348, Issue 1, 2006, Pages 47-55

Identification of a new in vivo phosphorylation site in the cytoplasmic carboxyl terminus of EBV-LMP1 by tandem mass spectrometry

Author keywords

Latent membrane protein 1; Mass spectrometry; Phosphorylation

Indexed keywords

AMINO ACID; GLUTATHIONE TRANSFERASE; LATENT MEMBRANE PROTEIN 1;

EID: 33746793620     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.188     Document Type: Article
Times cited : (6)

References (41)
  • 3
    • 22344443201 scopus 로고    scopus 로고
    • Involvement of the Epstein-Barr virus in the nasopharyngeal carcinoma pathogenesis
    • Burgos J.S. Involvement of the Epstein-Barr virus in the nasopharyngeal carcinoma pathogenesis. Med. Oncol. 22 (2005) 113-121
    • (2005) Med. Oncol. , vol.22 , pp. 113-121
    • Burgos, J.S.1
  • 4
    • 0037333399 scopus 로고    scopus 로고
    • Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis
    • Coffin III W.F., Geiger T.R., and Martin J.M. Transmembrane domains 1 and 2 of the latent membrane protein 1 of Epstein-Barr virus contain a lipid raft targeting signal and play a critical role in cytostasis. J. Virol. 77 (2003) 3749-3758
    • (2003) J. Virol. , vol.77 , pp. 3749-3758
    • Coffin III, W.F.1    Geiger, T.R.2    Martin, J.M.3
  • 5
    • 0037938602 scopus 로고    scopus 로고
    • LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments
    • Lam N., and Sugden B. LMP1, a viral relative of the TNF receptor family, signals principally from intracellular compartments. EMBO J. 22 (2003) 3027-3038
    • (2003) EMBO J. , vol.22 , pp. 3027-3038
    • Lam, N.1    Sugden, B.2
  • 6
    • 0036827830 scopus 로고    scopus 로고
    • LMP-1's transmembrane domains encode multiple functions required for LMP-1's efficient signaling
    • Kaykas A., Worringer K., and Sugden B. LMP-1's transmembrane domains encode multiple functions required for LMP-1's efficient signaling. J. Virol. 76 (2002) 11551-11560
    • (2002) J. Virol. , vol.76 , pp. 11551-11560
    • Kaykas, A.1    Worringer, K.2    Sugden, B.3
  • 7
    • 0027502911 scopus 로고
    • Biochemical, genetic, and functional analyses of the phosphorylation sites on the Epstein-Barr virus-encoded oncogenic latent membrane protein LMP-1
    • Moorthy R.K., and Thorley-Lawson D.A. Biochemical, genetic, and functional analyses of the phosphorylation sites on the Epstein-Barr virus-encoded oncogenic latent membrane protein LMP-1. J. Virol. 67 (1993) 2637-2645
    • (1993) J. Virol. , vol.67 , pp. 2637-2645
    • Moorthy, R.K.1    Thorley-Lawson, D.A.2
  • 8
    • 13844299238 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by mass spectrometry
    • Garcia B.A., Shabanowitz J., and Hunt D.F. Analysis of protein phosphorylation by mass spectrometry. Methods 35 (2005) 256-264
    • (2005) Methods , vol.35 , pp. 256-264
    • Garcia, B.A.1    Shabanowitz, J.2    Hunt, D.F.3
  • 9
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann M., Ong S.E., Gronborg M., Steen H., Jensen O.N., and Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20 (2002) 261-268
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 10
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H., Watts J.D., and Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19 (2001) 375-378
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 11
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y., Nagasu T., and Chait B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19 (2001) 379-382
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 12
    • 2342544898 scopus 로고    scopus 로고
    • Exploring the phosphoproteome with mass spectrometry
    • Peters E.C., Brock A., and Ficarro S.B. Exploring the phosphoproteome with mass spectrometry. Mini Rev. Med. Chem. 4 (2004) 313-324
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 313-324
    • Peters, E.C.1    Brock, A.2    Ficarro, S.B.3
  • 13
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F., and Pinna L.A. One-thousand-and-one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 14
    • 15244360230 scopus 로고    scopus 로고
    • Application of metal-chelate affinity chromatography to the study of the phosphoproteome
    • Imam-Sghiouar N., Joubert-Caron R., and Caron M. Application of metal-chelate affinity chromatography to the study of the phosphoproteome. Amino Acids 28 (2005) 105-109
    • (2005) Amino Acids , vol.28 , pp. 105-109
    • Imam-Sghiouar, N.1    Joubert-Caron, R.2    Caron, M.3
  • 16
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y., Nagasu T., and Chait B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19 (2001) 379-382
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 18
    • 24044455639 scopus 로고    scopus 로고
    • Systematic analysis of the epidermal growth factor receptor by mass spectrometry reveals stimulation-dependent multisite phosphorylation
    • Boeri E.E., Bergatto E., Cabodi S., Silengo L., Tarone G., Defilippi P., and Jensen O.N. Systematic analysis of the epidermal growth factor receptor by mass spectrometry reveals stimulation-dependent multisite phosphorylation. Mol. Cell. Proteomics 4 (2005) 1107-1121
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1107-1121
    • Boeri, E.E.1    Bergatto, E.2    Cabodi, S.3    Silengo, L.4    Tarone, G.5    Defilippi, P.6    Jensen, O.N.7
  • 19
    • 5444230640 scopus 로고    scopus 로고
    • Dynamic identification of phosphopeptides using immobilized metal ion affinity chromatography enrichment, subsequent partial beta-elimination/chemical tagging and matrix-assisted laser desorption/ionization mass spectrometric analysis
    • Ahn Y.H., Park E.J., Cho K., Kim J.Y., Ha S.H., Ryu S.H., and Yoo J.S. Dynamic identification of phosphopeptides using immobilized metal ion affinity chromatography enrichment, subsequent partial beta-elimination/chemical tagging and matrix-assisted laser desorption/ionization mass spectrometric analysis. Rapid Commun. Mass Spectrom. 18 (2004) 2495-2501
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 2495-2501
    • Ahn, Y.H.1    Park, E.J.2    Cho, K.3    Kim, J.Y.4    Ha, S.H.5    Ryu, S.H.6    Yoo, J.S.7
  • 20
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signaling pathways
    • Pandey A., Andersen J.S., and Mann M. Use of mass spectrometry to study signaling pathways. Sci. STKE 2000 (2000) L1
    • (2000) Sci. STKE , vol.2000
    • Pandey, A.1    Andersen, J.S.2    Mann, M.3
  • 22
    • 27144470222 scopus 로고    scopus 로고
    • Application of immobilized metal affinity chromatography in proteomics
    • Sun X., Chiu J.F., and He Q.Y. Application of immobilized metal affinity chromatography in proteomics. Expert Rev. Proteomics 2 (2005) 649-657
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 649-657
    • Sun, X.1    Chiu, J.F.2    He, Q.Y.3
  • 23
    • 12944318812 scopus 로고    scopus 로고
    • Reduction of non-specific binding in Ga(III) immobilized metal affinity chromatography for phosphopeptides by using endoproteinase glu-C as the digestive enzyme
    • Seeley E.H., Riggs L.D., and Regnier F.E. Reduction of non-specific binding in Ga(III) immobilized metal affinity chromatography for phosphopeptides by using endoproteinase glu-C as the digestive enzyme. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 817 (2005) 81-88
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.817 , pp. 81-88
    • Seeley, E.H.1    Riggs, L.D.2    Regnier, F.E.3
  • 24
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar V., and Menart V. Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49 (2001) 335-360
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 25
    • 0036295769 scopus 로고    scopus 로고
    • Identification of protein kinase CK2 as a potent kinase of Epstein-Barr virus latent membrane protein 1
    • Chi L.M., Yu J.S., and Chang Y.S. Identification of protein kinase CK2 as a potent kinase of Epstein-Barr virus latent membrane protein 1. Biochem. Biophys. Res. Commun. 294 (2002) 586-591
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 586-591
    • Chi, L.M.1    Yu, J.S.2    Chang, Y.S.3
  • 27
    • 1542465183 scopus 로고    scopus 로고
    • Interaction of Epstein-Barr virus latent membrane protein 1 with SCFHOS/beta-TrCP E3 ubiquitin ligase regulates extent of NF-kappaB activation
    • Tang W., Pavlish O.A., Spiegelman V.S., Parkhitko A.A., and Fuchs S.Y. Interaction of Epstein-Barr virus latent membrane protein 1 with SCFHOS/beta-TrCP E3 ubiquitin ligase regulates extent of NF-kappaB activation. J. Biol. Chem. 278 (2003) 48942-48949
    • (2003) J. Biol. Chem. , vol.278 , pp. 48942-48949
    • Tang, W.1    Pavlish, O.A.2    Spiegelman, V.S.3    Parkhitko, A.A.4    Fuchs, S.Y.5
  • 28
    • 0041335560 scopus 로고    scopus 로고
    • Ubiquitination of the Epstein-Barr virus-encoded latent membrane protein 1 depends on the integrity of the TRAF binding site
    • Rothenberger S., Burns K., Rousseaux M., Tschopp J., and Bron C. Ubiquitination of the Epstein-Barr virus-encoded latent membrane protein 1 depends on the integrity of the TRAF binding site. Oncogene 22 (2003) 5614-5618
    • (2003) Oncogene , vol.22 , pp. 5614-5618
    • Rothenberger, S.1    Burns, K.2    Rousseaux, M.3    Tschopp, J.4    Bron, C.5
  • 29
    • 0034604520 scopus 로고    scopus 로고
    • Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue
    • Aviel S., Winberg G., Massucci M., and Ciechanover A. Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue. J. Biol. Chem. 275 (2000) 23491-23499
    • (2000) J. Biol. Chem. , vol.275 , pp. 23491-23499
    • Aviel, S.1    Winberg, G.2    Massucci, M.3    Ciechanover, A.4
  • 30
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang G., Spellman D.S., Skolnik E.Y., and Neubert T.A. Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J. Proteome Res. 5 (2006) 581-588
    • (2006) J. Proteome Res. , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 31
    • 33644675365 scopus 로고    scopus 로고
    • Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications
    • Amanchy R., Kalume D.E., and Pandey A. Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications. Sci. STKE 2005 (2005) l2
    • (2005) Sci. STKE , vol.2005
    • Amanchy, R.1    Kalume, D.E.2    Pandey, A.3
  • 32
    • 0023369137 scopus 로고
    • An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes
    • Liebowitz D., Kopan R., Fuchs E., Sample J., and Kieff E. An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes. Mol. Cell. Biol. 7 (1987) 2299-2308
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2299-2308
    • Liebowitz, D.1    Kopan, R.2    Fuchs, E.3    Sample, J.4    Kieff, E.5
  • 33
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F., and Pinna L.A. One-thousand-and-one substrates of protein kinase CK2?. FASEB J. 17 (2003) 349-368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 34
    • 0035677840 scopus 로고    scopus 로고
    • HIV-1 Rev transactivator: a beta-subunit directed substrate and effector of protein kinase CK2
    • Meggio F., Marin O., Boschetti M., Sarno S., and Pinna L.A. HIV-1 Rev transactivator: a beta-subunit directed substrate and effector of protein kinase CK2. Mol. Cell. Biochem. 227 (2001) 145-151
    • (2001) Mol. Cell. Biochem. , vol.227 , pp. 145-151
    • Meggio, F.1    Marin, O.2    Boschetti, M.3    Sarno, S.4    Pinna, L.A.5
  • 35
    • 3142726432 scopus 로고    scopus 로고
    • Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta
    • El-Guindy A.S., and Miller G. Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta. J. Virol. 78 (2004) 7634-7644
    • (2004) J. Virol. , vol.78 , pp. 7634-7644
    • El-Guindy, A.S.1    Miller, G.2
  • 36
    • 0038340907 scopus 로고    scopus 로고
    • The raison d'etre of constitutively active protein kinases: the lesson of CK2
    • Pinna L.A. The raison d'etre of constitutively active protein kinases: the lesson of CK2. Acc. Chem. Res. 36 (2003) 378-384
    • (2003) Acc. Chem. Res. , vol.36 , pp. 378-384
    • Pinna, L.A.1
  • 37
    • 0025113220 scopus 로고
    • Casein kinase 2: an 'eminence grise' in cellular regulation?
    • Pinna L.A. Casein kinase 2: an 'eminence grise' in cellular regulation?. Biochim. Biophys. Acta 1054 (1990) 267-284
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 38
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • Meggio F., Marin O., and Pinna L.A. Substrate specificity of protein kinase CK2. Cell. Mol. Biol. Res. 40 (1994) 401-409
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 401-409
    • Meggio, F.1    Marin, O.2    Pinna, L.A.3
  • 39
    • 0033059744 scopus 로고    scopus 로고
    • Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable
    • McKendrick L., Milne D., and Meek D. Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable. Mol. Cell. Biochem. 191 (1999) 187-199
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 187-199
    • McKendrick, L.1    Milne, D.2    Meek, D.3
  • 40
    • 27144542052 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 CTAR1 mediates rodent and human fibroblast transformation through activation of PI3K
    • Mainou B.A., Everly Jr. D.N., and Raab-Traub N. Epstein-Barr virus latent membrane protein 1 CTAR1 mediates rodent and human fibroblast transformation through activation of PI3K. Oncogene 24 (2005) 6917-6924
    • (2005) Oncogene , vol.24 , pp. 6917-6924
    • Mainou, B.A.1    Everly Jr., D.N.2    Raab-Traub, N.3
  • 41
    • 6344272092 scopus 로고    scopus 로고
    • Roles of TNF receptor-associated factor 3 in signaling to B lymphocytes by carboxyl-terminal activating regions 1 and 2 of the EBV-encoded oncoprotein latent membrane protein 1
    • Xie P., and Bishop G.A. Roles of TNF receptor-associated factor 3 in signaling to B lymphocytes by carboxyl-terminal activating regions 1 and 2 of the EBV-encoded oncoprotein latent membrane protein 1. J. Immunol. 173 (2004) 5546-5555
    • (2004) J. Immunol. , vol.173 , pp. 5546-5555
    • Xie, P.1    Bishop, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.